Lamin B1 sequesters 53BP1 to control its recruitment to DNA damage
Open accessAbstract
Double-strand breaks (DSBs) are harmful lesions and a major cause of genome instability. Studies have suggested a link between the nuclear envelope and the DNA damage response. Here, we show that lamin B1, a major component of the nuclear envelope, interacts directly with 53BP1 protein, which plays a pivotal role in the DSB repair. This interaction is dissociated after DNA damage. Lamin B1 overexpression impedes 53BP1 recruitment to DNA damage sites and leads to a persistence of DNA damage, a defect in nonhomologous end joining and an increased sensitivity to DSBs. The identification of interactions domains between lamin B1 and 53BP1 allows us to demonstrate that the defect of 53BP1 recruitment and the DSB persistence upon lamin B1 overexpression are due to sequestration of 53BP1 by lamin B1. This study highlights lamin B1 as a factor controlling the recruitment of 53BP1 to DNA damage sites upon injury.
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Lamin B1 controls release of DSB repair protein 53BP1 and overexpression of Lamin B1 impedes DSB repair leading to persistent DSBs.
“Lamin B1 has been shown to control the release of DSB repair protein 53BP1 and overexpression of LaminB1 impeded DSB repair leading to persistent DSBs”
From Neuronal DNA double-strand breaks lead to genome structural variations and 3D genome disruption in neurodegeneration (2023) · cites this paper as [88]
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- Authors
- Etourneaud, L., Moussa, A., Rass, E., Genet, D., Willaume, S., Chabance-Okumura, C., Wanschoor, P., Picotto, J., Thézé, B., Dépagne, J., Veaute, X., Dizet, E., Busso, D., Barascu, A., Irbah, L., Kortulewski, T., Campalans, A., Le Chalony, C., Zinn-Justin, S., Scully, R., Pennarun, G., & Bertrand, P.
- Affiliations
- Inserm (FR)
- Université de Paris and Université Paris Saclay, INSERM, iRCM/IBFJ, CEA, UMR Stabilité Génétique, Cellules Souches et Radiations, F-92265 Fontenay-aux-Roses, France.
- Commissariat à l'Énergie Atomique et aux Énergies Alternatives (FR)
- Laboratory of Structural Biology and Radiobiology, Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Saclay, F-91190 Gif-sur-Yvette, France.
- Beth Israel Deaconess Medical Center (US)
- Corresponding author
- Etourneaud, Laure
- Moussa, Angela
- Rass, Emilie
- Genet, Diane
- Bertrand, Pascale
- ORCID
- Venue
- Science Advances
- Published
- 2021-08-27
- Volume
- 7
- Issue
- 35
- ISSN
- 2375-2548 (ISSN-L)
- PMC
- PMC8397269
- OpenAlex
- W3194798061
- Cited by
- 54
- References
- 76
- Citations by year
- 2026: 9 · 2025: 17 · 2024: 7 · 2023: 13 · 2022: 7 · 2021: 1
- FWCI
- 2.20
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Science Advances (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- Louisville Institute
- Fondation ARC pour la Recherche sur le Cancer (ARCPJA32020070002430)
- Ligue Contre le Cancer (comité Ile de France)
- INSERM (house funding- Unit SGCSR)
- INCA
- Fondation pour la Recherche Medicale
- AT europe
- Ligue Contre le Cancer fellowship
- CEA Radiobiology segment grant
- AFM-Téléton (n◦21566)
- CEA Irtelis fellowship
- Fondation ARC fellowship
- CEA DRF “Phare” fellowship
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Effects of Radiation Exposure
- Keywords
- lamin B1, 53BP1, DNA damage response, DNA double-strand break repair, non-homologous end joining, nuclear envelope, protein-protein interaction, genomic instability, protein sequestration
- MeSH terms
- Tumor Suppressor p53-Binding Protein 1, DNA Damage, Lamin Type B, DNA Breaks, Double-Stranded, DNA End-Joining Repair
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